› 2ds8

X-ray diffraction
1.6Å resolution

Structure of the ZBD-XB complex

Released:
DOI: 10.2210/pdb2ds8/pdb
PDB entry 2ds8 coloured by chain, front view.
PDB entry 2ds8 coloured by chain, side view.
PDB entry 2ds8 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural basis of SspB-tail recognition by the zinc binding domain of ClpX.
Park EY, Lee BG, Hong SB, Kim HW, Jeon H, Song HK
J Mol Biol 367 514-26 (2007)
PMID: 17258768

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141342 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-dependent Clp protease ATP-binding subunit ClpX Chains: A, B
Molecule details ›
Chains: A, B
Length: 51 amino acids
Theoretical weight: 5.76 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A6H1 (Residues: 2-52; Coverage: 12%)
Gene names: JW0428, b0438, clpX, lopC
Sequence domains: ClpX C4-type zinc finger
Structure domains: ClpX chaperone, C4-type zinc finger domain
SspB-tail peptide Chains: P, Q
Molecule details ›
Chains: P, Q
Length: 8 amino acids
Theoretical weight: 855 Da
Source organism: Escherichia coli
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P212121
Unit cell:
a: 32.554Å b: 46.548Å c: 57.037Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.201 0.226
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

7 review citations

ClpXP, an ATP-powered unfolding and protein-degradation machine.
Baker et al. (2012)
6 more

7 mentions without citation

High-resolution global peptide-protein docking using fragments-based PIPER-FlexPepDock.
Alam et al. (2017)
6 more